HMM Summary Page: TIGR02484

FunctionCitB domain protein
Trusted Cutoff246.60
Domain Trusted Cutoff246.60
Noise Cutoff166.20
Domain Noise Cutoff166.20
Isology Typesubfamily_domain
HMM Length372
AuthorSelengut J
Entry DateFeb 24 2005 8:04AM
Last ModifiedFeb 14 2011 3:27PM
CommentThis model identifies proteins of two distinct names which may or may not have two distinct functions. CitB [1] has been identified in salmonella and E. coli as the signal transduction component of a two-component system for citrate in which CitA acts as a citrate transporter. CobZ is essential for cobalamin biosynthesis (by knockout of the R. capsulatus gene [2]) and is complemented by the characterized precorrin 3B synthase CobG. The enzyme has been shown to contain flavin, heme and Fe-S cluster cofactors and is believed to require dioxygen as a substrate. This model identifies the C-terminal domain of the R. capsulatus CobZ, which, in most other species exists as a separate gene adjacent to CobZ.
ReferencesRN [1] RM PMID: 1718953 RT Cloning and nucleotide sequence of the gene (citA) encoding a citrate carrier from Salmonella typhimurium. RA Shimamoto T, Izawa H, Daimon H, Ishiguro N, Shinagawa M, Sakano Y, Tsuda M, Tsuchiya T. RL J Biochem (Tokyo). 1991 Jul;110(1):22-8. RN [2] RM PMID: 15525640 RT Identification and characterization of a novel vitamin B12 (cobalamin) biosynthetic enzyme (CobZ) from Rhodobacter capsulatus, containing flavin, heme, and Fe-S cofactors. RA McGoldrick HM, Roessner CA, Raux E, Lawrence AD, McLean KJ, Munro AW, Santabarbara S, Rigby SE, Heathcote P, Scott AI, Warren MJ. RL J Biol Chem. 2005 Jan 14;280(2):1086-94. Epub 2004 Nov 03.